ArticleThe Journal of biological chemistry2012
Electrostatic ratchet in the protective antigen channel promotes anthrax toxin translocation.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 48 citations in OpenAlex.
- Structural basis for independent pore function of Vpb4 from Bacillus thuringiensis.Nature communications · 2026Article
- Structural basis for the assembly and translocation of the Vip1-Vip2 insecticidal toxin from Bacillus thuringiensis.Nature communications · 2026Article
- Peptide properties predict multistate translocation kinetics via protective antigen nanopores.Biophysical journal · 2026Article
- Dynamic gating by ϕ-clamp loop controls peptide translocation through the anthrax toxin nanopore.Biophysical journal · 2026Article
- A dynamical anthrax toxin nanopore biosensor for high-fidelity single-peptide classification.PLoS computational biology · 2026Article
- The N-terminus of themBio · 2025Article
- Deep learning-based classification of peptide analytes from single-channel nanopore translocation events.PloS one · 2025Article
- Anthrax toxin translocation complex reveals insight into the lethal factor unfolding and refolding mechanism.Scientific reports · 2021Article
- Atomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors.Structure (London, England : 1993) · 2020Article
- Cryo-EM structure of the fully-loaded asymmetric anthrax lethal toxin in its heptameric pre-pore state.PLoS pathogens · 2020Article
- Cryo-EM structures reveal translocational unfolding in the clostridial binary iota toxin complex.Nature structural & molecular biology · 2020Article
- Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors.Nature communications · 2020Article
- Structural insights into the transition of Clostridioides difficile binary toxin from prepore to pore.Nature microbiology · 2020Article
- Advances in cryoEM and its impact on β-pore forming proteins.Current opinion in structural biology · 2018Review
- Asymmetric Cryo-EM Structure of Anthrax Toxin Protective Antigen Pore with Lethal Factor N-Terminal Domain.Toxins · 2017Article
- Dynamic Phenylalanine Clamp Interactions Define Single-Channel Polypeptide Translocation through the Anthrax Toxin Protective Antigen Channel.Journal of molecular biology · 2017Article
- Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry.The Journal of general physiology · 2016Article
- Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Forces from the Portal Govern the Late-Stage DNA Transport in a Viral DNA Packaging Nanomotor.Biophysical journal · 2016Article
- Molecular assembly of lethal factor enzyme and pre-pore heptameric protective antigen in early stage of translocation.Journal of molecular modeling · 2016Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Central to the power-stroke and brownian-ratchet mechanisms of protein translocation is the process through which nonequilibrium fluctuations are rectified or ratcheted by the molecular motor to transport substrate proteins along a specific axis. We investigated the ratchet mechanism using anthrax toxin as a model. Anthrax toxin is a tripartite toxin comprised of the protective antigen (PA) component, a homooligomeric transmembrane translocase, which translocates two other enzyme components, lethal factor (LF) and edema factor (EF), into the cytosol of the host cell under the proton motive force (PMF). The PA-binding domains of LF and EF (LF(N) and EF(N)) possess identical folds and similar solution stabilities; however, EF(N) translocates ∼10-200-fold slower than LF(N), depending on the electrical potential (Δψ) and chemical potential (ΔpH) compositions of the PMF. From an analysis of LF(N)/EF(N) chimera proteins, we identified two 10-residue cassettes comprised of charged sequence that were responsible for the impaired translocation kinetics of EF(N). These cassettes have nonspecific electrostatic requirements: one surprisingly prefers acidic residues when driven by either a Δψ or a ΔpH; the second requires basic residues only when driven by a Δψ. Through modeling and experiment, we identified a charged surface in the PA channel responsible for charge selectivity. The charged surface latches the substrate and promotes PMF-driven transport. We propose an electrostatic ratchet in the channel, comprised of opposing rings of charged residues, enforces directionality by interacting with charged cassettes in the substrate, thereby generating forces sufficient to drive unfolding.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.